Fig. 4: Cryo-EM structure of apo-MET1full.
a Cryo-EM density map (left) and cartoon model (right) of apo-MET1full. Zinc ion is shown as red sphere. The disordered acidic-linker is indicated by the green dotted lines. b Structural alignment between apo-MET1full (cyan) and MET1MTase bound to hmDNA (gray). c A close-up view of the RFTS2 domain and hmDNA in Fig. 4b. hmDNA is shown as a gray stick model overlaying the cryo-EM map. The sterically hindered region of the N-lobe of the RFTS2 domain is shown in orange. d A close-up view of the connecting linker (red) and hmDNA (gray) in Fig. 4b. e The left panel displays the structure of the RFTS2 domain, depicted as the salmon surface, bound to the connecting linker (red) and the TRD (orange). The right panel shows the structure around the Toggle Pocket (light yellow) of apo-MET1full. The Toggle Pocket is shown as a stick model with a transparent sphere model. Residues in the Activating Helix and DNA Recognition Helix are shown as green and magenta stick models, respectively.
